ID A0A0D2ADU8_9EURO Unreviewed; 597 AA.
AC A0A0D2ADU8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000256|ARBA:ARBA00033770};
DE EC=2.4.2.14 {ECO:0000256|ARBA:ARBA00011941};
DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000256|ARBA:ARBA00033776};
GN ORFNames=PV06_09323 {ECO:0000313|EMBL:KIW38351.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW38351.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW38351.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW38351.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC diphosphate: step 1/2. {ECO:0000256|ARBA:ARBA00005209}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC phosphoribosyltransferase family. {ECO:0000256|ARBA:ARBA00010138}.
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DR EMBL; KN847341; KIW38351.1; -; Genomic_DNA.
DR RefSeq; XP_016258567.1; XM_016410760.1.
DR AlphaFoldDB; A0A0D2ADU8; -.
DR STRING; 215243.A0A0D2ADU8; -.
DR GeneID; 27361397; -.
DR VEuPathDB; FungiDB:PV06_09323; -.
DR HOGENOM; CLU_022389_2_1_1; -.
DR OrthoDB; 4975at2759; -.
DR UniPathway; UPA00074; UER00124.
DR Proteomes; UP000053342; Unassembled WGS sequence.
DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR CDD; cd00715; GPATase_N; 1.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR HAMAP; MF_01931; PurF; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005854; PurF.
DR InterPro; IPR035584; PurF_N.
DR NCBIfam; TIGR01134; purF; 1.
DR PANTHER; PTHR11907; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11907:SF0; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF13522; GATase_6; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:KIW38351.1};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000053342};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:KIW38351.1}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..597
FT /note="Amidophosphoribosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002238405"
FT DOMAIN 2..242
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 544..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 65062 MW; 5D11A99632C71DCE CRC64;
MCGILALILA NSASTSAAID LHEALYLLQH RGQDACGIAT CASGGRIYQC KGNGMAAKVF
HDGSRVIDLP GFMGLGHLRY PTAGSSANAE AQPFYVNSPY GLCLAHNGNL INAPELKRYL
DREAHRHINT DSDSELMLNI FANELNETGK ARVNDDDVFA ALSRMYDKCQ GGWACTAMIA
GYGLIGFRDS YGIRPLVLGS RDSVDGHGKD YMMASESVAL AQLGFDVIRD ILPGEAVILQ
KGHAPHFRQV QERRSYAPDI FEYVYFARPD SVMDGISVHR SRQHMGSRLA EEVRRVLSPQ
DLADIDVVIP IPETSVTSAA VVAKALDKEY CQGFVKNRYV FRTFIMPEQK ARQKGVRRKL
NAMAMEFKDR NVLLVDDSIV RGTTSREIVT MAREAGAKKV HFASCAPPIT HAHIYGIDLA
SPFELVAHNH HGTEAIAKHI GADSVIFQTL DDLKAACVDA AREAHSQDAP NDFEVGVFCG
SYITPVNQSY FDHLERVRGQ TRRLKVMDEA RRAVAQGVAG EDQINMAANG AVITERGKVV
PAANGEARRS SVHVNGSDAF GHDAAAETAP APSQEDESPS VRDRMDISLH NLGDFPG
//
